The role of (auto)-phosphorylation in the complex activation mechanism of LRRK2Athanasopoulos, P. S., Heumann, R. & Kortholt, A., Jul-2018, In : Biological Chemistry. 399, 7, p. 643-647 5 p.
Research output: Contribution to journal › Article › Academic › peer-review
Mutations in human leucine-rich-repeat kinase 2 (LRRK2) have been found to be the most frequent cause of late-onset Parkinson's Disease (PD). LRRK2 is a large protein with two enzymatic domains, a GTPase and a kinase domain. A cluster of (auto)-phosphorylation sites within the N-terminus of LRRK2 have been shown to be crucial for the localization of LRRK2 and is important for PD pathogenesis. In addition, phosphorylation of sites within the G-domain of the protein affect GTPase activity. Here we discuss the role of these (auto)-phosphorylation sites of LRRK2 and their regulation by phosphatases and upstream kinases.
|Number of pages||5|
|Early online date||12-Mar-2018|
|Publication status||Published - Jul-2018|
|Event||Conference on Molecular Basis of Life - Bochum, Germany|
Duration: 1-Sep-2017 → …
Conference on Molecular Basis of Life
01/09/2017 → …Bochum, Germany
- GTPase, kinase, neuronal degeneration, Parkinson's disease, phosphatases, DISEASE-ASSOCIATED MUTATIONS, SYNAPTIC VESICLE TRAFFICKING, REPEAT KINASE 2, PARKINSONS-DISEASE, GTP-BINDING, CYTOPLASMIC LOCALIZATION, PHOSPHORYLATION, PENETRANCE, PHENOTYPE, PROTEINS